JP2013531651A5 - - Google Patents
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- JP2013531651A5 JP2013531651A5 JP2013514555A JP2013514555A JP2013531651A5 JP 2013531651 A5 JP2013531651 A5 JP 2013531651A5 JP 2013514555 A JP2013514555 A JP 2013514555A JP 2013514555 A JP2013514555 A JP 2013514555A JP 2013531651 A5 JP2013531651 A5 JP 2013531651A5
- Authority
- JP
- Japan
- Prior art keywords
- seq
- thrombomodulin
- analog
- amino acid
- motomeko
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
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- 108010079274 Thrombomodulin Proteins 0.000 claims description 70
- 102100026966 Thrombomodulin Human genes 0.000 claims description 70
- 150000001413 amino acids Chemical group 0.000 claims description 43
- 235000001014 amino acid Nutrition 0.000 claims description 31
- 230000000694 effects Effects 0.000 claims description 26
- COLNVLDHVKWLRT-QMMMGPOBSA-N phenylalanine group Chemical group N[C@@H](CC1=CC=CC=C1)C(=O)O COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 22
- 229940024606 amino acid Drugs 0.000 claims description 21
- 206010053567 Coagulopathies Diseases 0.000 claims description 18
- 208000015294 blood coagulation disease Diseases 0.000 claims description 18
- 229960000301 factor viii Drugs 0.000 claims description 16
- 108010054218 Factor VIII Proteins 0.000 claims description 15
- 102000001690 Factor VIII Human genes 0.000 claims description 15
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical class CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 15
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 claims description 14
- 230000009852 coagulant defect Effects 0.000 claims description 13
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical class CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 12
- 238000011282 treatment Methods 0.000 claims description 12
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 11
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Chemical compound CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 11
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical class NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 10
- 108090000190 Thrombin Proteins 0.000 claims description 10
- 238000006467 substitution reaction Methods 0.000 claims description 10
- 229960004072 thrombin Drugs 0.000 claims description 10
- 101100118545 Holotrichia diomphalia EGF-like gene Proteins 0.000 claims description 9
- 230000004048 modification Effects 0.000 claims description 9
- 238000012986 modification Methods 0.000 claims description 9
- 102100035023 Carboxypeptidase B2 Human genes 0.000 claims description 8
- 108090000201 Carboxypeptidase B2 Proteins 0.000 claims description 8
- 208000032843 Hemorrhage Diseases 0.000 claims description 8
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 claims description 8
- 230000000740 bleeding effect Effects 0.000 claims description 7
- 230000004913 activation Effects 0.000 claims description 6
- 235000004279 alanine Nutrition 0.000 claims description 6
- 238000012217 deletion Methods 0.000 claims description 6
- 230000037430 deletion Effects 0.000 claims description 6
- 238000000034 method Methods 0.000 claims description 6
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 6
- 230000020764 fibrinolysis Effects 0.000 claims description 5
- 108010089996 B-domain-deleted factor VIII Proteins 0.000 claims description 4
- 239000004471 Glycine Substances 0.000 claims description 4
- -1 His Chemical compound 0.000 claims description 4
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims description 4
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical class C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims description 4
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Chemical class CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 4
- 241000283973 Oryctolagus cuniculus Species 0.000 claims description 4
- 101100226846 Strongylocentrotus purpuratus EGF3 gene Proteins 0.000 claims description 4
- 208000027276 Von Willebrand disease Diseases 0.000 claims description 4
- 230000037396 body weight Effects 0.000 claims description 4
- 239000012634 fragment Substances 0.000 claims description 4
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims description 4
- 229960000310 isoleucine Drugs 0.000 claims description 4
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Chemical class CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 4
- 210000004072 lung Anatomy 0.000 claims description 4
- JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 claims description 4
- 208000012137 von Willebrand disease (hereditary or acquired) Diseases 0.000 claims description 4
- 102000015081 Blood Coagulation Factors Human genes 0.000 claims description 3
- 108010039209 Blood Coagulation Factors Proteins 0.000 claims description 3
- 208000009292 Hemophilia A Diseases 0.000 claims description 3
- 239000003114 blood coagulation factor Substances 0.000 claims description 3
- 208000015957 Acquired Von Willebrand disease Diseases 0.000 claims description 2
- 101100129088 Caenorhabditis elegans lys-2 gene Proteins 0.000 claims description 2
- 102100022641 Coagulation factor IX Human genes 0.000 claims description 2
- 102100026735 Coagulation factor VIII Human genes 0.000 claims description 2
- 102100037642 Elongation factor G, mitochondrial Human genes 0.000 claims description 2
- 201000003542 Factor VIII deficiency Diseases 0.000 claims description 2
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 claims description 2
- 101000880344 Homo sapiens Elongation factor G, mitochondrial Proteins 0.000 claims description 2
- 101000763314 Homo sapiens Thrombomodulin Proteins 0.000 claims description 2
- 101000938391 Homo sapiens Transmembrane protein Proteins 0.000 claims description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical group CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 2
- 230000003213 activating effect Effects 0.000 claims description 2
- 238000010171 animal model Methods 0.000 claims description 2
- 239000003130 blood coagulation factor inhibitor Substances 0.000 claims description 2
- VDQQXEISLMTGAB-UHFFFAOYSA-N chloramine T Chemical compound [Na+].CC1=CC=C(S(=O)(=O)[N-]Cl)C=C1 VDQQXEISLMTGAB-UHFFFAOYSA-N 0.000 claims description 2
- 108010009717 circulating anticoagulants Proteins 0.000 claims description 2
- 230000015271 coagulation Effects 0.000 claims description 2
- 238000005345 coagulation Methods 0.000 claims description 2
- 208000011664 congenital factor XI deficiency Diseases 0.000 claims description 2
- 230000009089 cytolysis Effects 0.000 claims description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 2
- 239000003814 drug Substances 0.000 claims description 2
- 238000000605 extraction Methods 0.000 claims description 2
- 208000005376 factor X deficiency Diseases 0.000 claims description 2
- 201000007219 factor XI deficiency Diseases 0.000 claims description 2
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 claims description 2
- 210000001035 gastrointestinal tract Anatomy 0.000 claims description 2
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 claims description 2
- 208000035474 group of disease Diseases 0.000 claims description 2
- 208000009429 hemophilia B Diseases 0.000 claims description 2
- 208000031169 hemorrhagic disease Diseases 0.000 claims description 2
- 238000000099 in vitro assay Methods 0.000 claims description 2
- 230000007774 longterm Effects 0.000 claims description 2
- 210000003205 muscle Anatomy 0.000 claims description 2
- 230000006318 protein oxidation Effects 0.000 claims description 2
- 238000009256 replacement therapy Methods 0.000 claims description 2
- 210000002345 respiratory system Anatomy 0.000 claims description 2
- 238000012216 screening Methods 0.000 claims description 2
- 210000004872 soft tissue Anatomy 0.000 claims description 2
- 238000001356 surgical procedure Methods 0.000 claims description 2
- 239000004474 valine Chemical group 0.000 claims description 2
- 239000000203 mixture Substances 0.000 claims 31
- 239000008280 blood Substances 0.000 claims 3
- 210000004369 blood Anatomy 0.000 claims 3
- 238000001990 intravenous administration Methods 0.000 claims 1
- 230000003647 oxidation Effects 0.000 claims 1
- 238000007254 oxidation reaction Methods 0.000 claims 1
- 210000000574 retroperitoneal space Anatomy 0.000 claims 1
- 238000007920 subcutaneous administration Methods 0.000 claims 1
- 208000034158 bleeding Diseases 0.000 description 5
- 208000031220 Hemophilia Diseases 0.000 description 1
- 230000001567 anti-fibrinolytic effect Effects 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| PCT/EP2010/003541 WO2010142461A2 (en) | 2009-06-12 | 2010-06-14 | Treatment of coagulopathy with hyperfibrinolysis |
| EPPCT/EP2010/003541 | 2010-06-14 | ||
| PCT/EP2010/007632 WO2011157283A1 (en) | 2010-06-14 | 2010-12-15 | Treatment of coagulopathy with hyperfibrinolysis |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2013531651A JP2013531651A (ja) | 2013-08-08 |
| JP2013531651A5 true JP2013531651A5 (enExample) | 2014-11-06 |
Family
ID=43857859
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2013514555A Pending JP2013531651A (ja) | 2010-06-14 | 2010-12-15 | 線溶亢進を伴う凝固障害の処置 |
Country Status (6)
| Country | Link |
|---|---|
| JP (1) | JP2013531651A (enExample) |
| CN (1) | CN103037893A (enExample) |
| AU (1) | AU2010355558A1 (enExample) |
| BR (1) | BR112012031920A2 (enExample) |
| CA (1) | CA2802072A1 (enExample) |
| WO (1) | WO2011157283A1 (enExample) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2620071C2 (ru) | 2010-11-17 | 2017-05-22 | Чугаи Сеияку Кабушики Каиша | Мультиспецифическая связывающая антиген молекула, которая обладает альтернативной функцией к функции фактора свертывания крови viii |
| TWI831106B (zh) * | 2014-06-20 | 2024-02-01 | 日商中外製藥股份有限公司 | 用於因第viii凝血因子及/或活化的第viii凝血因子的活性降低或欠缺而發病及/或進展的疾病之預防及/或治療之醫藥組成物 |
| TWI820000B (zh) | 2016-04-28 | 2023-11-01 | 日商中外製藥股份有限公司 | 含抗體製劑 |
| JP7125932B2 (ja) | 2016-09-06 | 2022-08-25 | 中外製薬株式会社 | 凝固第ｉｘ因子および／または活性化凝固第ｉｘ因子ならびに凝固第ｘ因子および／または活性化凝固第ｘ因子を認識する二重特異性抗体の使用法 |
| CN107083357B (zh) * | 2017-06-16 | 2021-04-02 | 四川农业大学 | 一种诱导培养骨髓间充质干细胞的方法 |
| JP2019031486A (ja) * | 2017-08-04 | 2019-02-28 | 公立大学法人福島県立医科大学 | 新規ポリペプチド及びその用途 |
| CN107677834B (zh) * | 2017-09-25 | 2019-07-09 | 辽宁迈迪生物科技股份有限公司 | TAFIa含量的检测方法、用于检测TAFIa含量的试剂盒及二者的应用 |
| AR113816A1 (es) | 2017-11-01 | 2020-06-17 | Chugai Pharmaceutical Co Ltd | Variantes e isoformas de anticuerpos con actividad biológica reducida |
| CN111961137B (zh) * | 2020-08-27 | 2023-09-05 | 南开大学 | 仿生内皮细胞功能的融合蛋白及其应用 |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3856335T2 (de) | 1987-01-08 | 2000-01-27 | Asahi Kasei Kogyo K.K., Osaka | Peptid zur beschleunigung der wirkung des proteins-c mit thrombin |
| US5256770A (en) | 1990-04-09 | 1993-10-26 | Schering Ag | Oxidation resistant thrombomodulin analogs |
| CA2648350A1 (en) | 1990-08-15 | 1992-03-05 | Schering Aktiengesellschaft | Superior thrombomodulin analogs for pharmaceutical use |
| EP1449849A3 (en) | 1992-02-05 | 2006-01-25 | Paion Deutschland GmbH | Protease-resistant thrombomodulin analog |
| WO1993025675A1 (en) * | 1992-06-10 | 1993-12-23 | Schering Aktiengesellschaft | Mutants of the epidermal growth factor domains of human thrombomodulin |
| EP1383885A4 (en) | 2001-04-04 | 2005-11-30 | American Diagnostica Inc | METHOD FOR PRODUCING A STABILIZED THROMBIN-ACTIVATED FIBRINOLYSE INHIBITOR (TAFI) AND METHOD FOR THE USE THEREOF |
| EP2104508A2 (en) * | 2006-12-12 | 2009-09-30 | Eli Lilly And Company | Treating acute renal failure with soluble thrombomodulin variants |
| AU2009347614A1 (en) * | 2009-06-12 | 2012-01-19 | Paion Deutschland Gmbh | Treatment of coagulopathy with hyperfibrinolysis |
-
2010
- 2010-12-15 CN CN201080068202XA patent/CN103037893A/zh active Pending
- 2010-12-15 BR BR112012031920A patent/BR112012031920A2/pt not_active IP Right Cessation
- 2010-12-15 CA CA2802072A patent/CA2802072A1/en not_active Abandoned
- 2010-12-15 AU AU2010355558A patent/AU2010355558A1/en not_active Abandoned
- 2010-12-15 WO PCT/EP2010/007632 patent/WO2011157283A1/en not_active Ceased
- 2010-12-15 JP JP2013514555A patent/JP2013531651A/ja active Pending
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